ID   Y1435_CLOAB             Reviewed;         456 AA.
AC   Q97J51;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Uncharacterized RNA methyltransferase CA_C1435;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=CA_C1435;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01024}.
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DR   EMBL; AE001437; AAK79403.1; -; Genomic_DNA.
DR   PIR; H97076; H97076.
DR   RefSeq; NP_348063.1; NC_003030.1.
DR   RefSeq; WP_010964744.1; NC_003030.1.
DR   AlphaFoldDB; Q97J51; -.
DR   SMR; Q97J51; -.
DR   STRING; 272562.CA_C1435; -.
DR   PRIDE; Q97J51; -.
DR   EnsemblBacteria; AAK79403; AAK79403; CA_C1435.
DR   GeneID; 44997941; -.
DR   KEGG; cac:CA_C1435; -.
DR   PATRIC; fig|272562.8.peg.1640; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_2_9; -.
DR   OMA; VLNCEFI; -.
DR   OrthoDB; 1421660at2; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..456
FT                   /note="Uncharacterized RNA methyltransferase CA_C1435"
FT                   /id="PRO_0000161969"
FT   DOMAIN          3..61
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         74
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         384
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   456 AA;  51312 MW;  2F163B07786725A0 CRC64;
     MKLMRKNETR EFLIEDIEFP AVGVAFYNDK KVYIKGAVPG QKVLARVSKV RREKIEAKLK
     EIVTNIPGAA QPKCPDFGVC GGCVHQFLPY EKQLEFKERE VLKLFKDAKI EGFEYLGILG
     SPEKEEYRNK MEYTFGDFVK GGELTLGMHA KNSGFSIVNT DKCNIVDEDF RIILKTVVEY
     FRKKDLPIYK VMQHVGYLRN LVVRKAKNTG EILIALVTTS QVDFDLTELT EILKSINYLG
     ELKGILHVIN DGLADMVRGD KIVTLFGQDY ITERILDLKF KISLFSFFQT NSKGAEKLYS
     EVLEFLGDVS NKTVFDLYCG TGTIGQLASK KAEKVIGIEL IEEAVEAAKE NTKLNNISNC
     SFIAGDVAKV ITEIKEKPDT IILDPPRPGV SPNAMKYVIK FNAPEIVYVS CNPKTLVNDL
     GVLRAYGYEV EKVKIVDMFP GTGHVETVVL LQRKII